ID D0LRK9_HALO1 Unreviewed; 463 AA.
AC D0LRK9;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:ACY19001.1};
GN OrderedLocusNames=Hoch_6532 {ECO:0000313|EMBL:ACY19001.1};
OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium.
OX NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY19001.1, ECO:0000313|Proteomes:UP000001880};
RN [1] {ECO:0000313|EMBL:ACY19001.1, ECO:0000313|Proteomes:UP000001880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2
RC {ECO:0000313|Proteomes:UP000001880};
RX PubMed=21304682; DOI=10.4056/sigs.69.1277;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A.,
RA Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F.,
RA Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A.,
RA Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Haliangium ochraceum type strain (SMP-2).";
RL Stand. Genomic Sci. 2:96-106(2010).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001804; ACY19001.1; -; Genomic_DNA.
DR RefSeq; WP_012831593.1; NC_013440.1.
DR AlphaFoldDB; D0LRK9; -.
DR STRING; 502025.Hoch_6532; -.
DR KEGG; hoh:Hoch_6532; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_4_1_7; -.
DR OrthoDB; 9811557at2; -.
DR Proteomes; UP000001880; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001880}.
FT DOMAIN 38..217
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 463 AA; 50406 MW; 6CEC81E727CAAEDD CRC64;
MSLPSEFLAV TKRDFPADFA TDDPEMLATY GVDWTRVFTP APSLVVRPRN TEEVARFISL
CHEHGVAVVP SGGRTGLAGG AVAKDGEVVV SLERMRRIDS VDENGMSVRV EAGAITEAVH
QHCAQLGLTW PVDFASKGSS QIGGNIATNA GGVKVIRYGL TRQWVLGLQV VTGTGEVLEL
GGALEKNNTG VDLRQLFIGS EGILGLVTEA TLKLTRLPER LDVFLFALDD LAAVLALFRA
ARRAPFQVSA YEFFTSRCLA RVRRHRAIDA PFHQPSPFYV LLEVEAHELD LLEDWLAGLF
DDGIVRDGVL AQTTAQARAL WELREAISES LAATGMPHKN DVALPIASLD AFCADLERVF
ADEYPTWEIC LFGHIGDGNL HVNVMKPDDL DKDSFLARTH EADAHLFELV RSYRGSVSAE
HGIGLLKRPW LGHTRSASEI ALMRALKSAL DPKGILNPGK VIG
//
